Research workbench
AlphaFold monomer V2.0 prediction for NA(+)/H(+) antiporter nhab (Q8DAG9)
Analyse AlphaFold monomer V2.0 prediction for NA(+)/H(+) antiporter nhab (Q8DAG9) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q8DAG9
- Type
- protein
- Length
- 529 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xD46bf19A439600e699da317abd477927C7884D8B
- Molecule
- NA(+)/H(+) antiporter nhab
- UniProt
- Q8DAG9
- Pockets
- 5 · best druggability 0.60
Structure
1 distinct chain · 75% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NA(+)/H(+) antiporter nhab | protein | 529 | 75% helix, 0% strand | Q8DAG9 |
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 115 | 0.60 | 0.85 | 18 | empty |
| 2 | 185 | 0.52 | 0.78 | 18 | empty |
| 3 | 185 | 0.45 | 0.75 | 19 | empty |
| 4 | 73 | 0.44 | 0.80 | 15 | empty |
| 5 | 65 | 0.32 | 0.75 | 15 | empty |
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q8DAG9
- Elsewhere: UniProt Q8DAG9 · AlphaFold DB Q8DAG9
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